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Protein Page:
MFN2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
MFN2 Essential transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. MFN2 acts independently of the cytoskeleton. It therefore plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes. Overexpression induces the formation of mitochondrial networks. Plays an important role in the regulation of vascular smooth muscle cell proliferation. Defects in MFN2 are the cause of Charcot-Marie-Tooth disease type 2A2 (CMT2A2). CMT2A2 is a form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathy or CMT1, and primary peripheral axonal neuropathy or CMT2. Neuropathies of the CMT2 group are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Defects in MFN2 are the cause of Charcot-Marie-Tooth disease type 6 (CMT6); also referred to as autosomal dominant hereditary motor and sensory neuropathy VI (HMSN6). CMT6 is an autosomal dominant form of axonal CMT associated with optic atrophy. Belongs to the mitofusin family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.5.-; Membrane protein, integral; Hydrolase; Mitochondrial; Membrane protein, multi-pass; Cell cycle regulation; Cytoskeletal protein
Cellular Component: microtubule cytoskeleton; mitochondrial outer membrane; mitochondrion; integral to membrane; cytosol; intrinsic to mitochondrial outer membrane
Molecular Function: GTPase activity; protein binding; GTP binding; ubiquitin protein ligase binding
Biological Process: cell death; camera-type eye morphogenesis; mitochondrial fusion; negative regulation of smooth muscle cell proliferation; GTP catabolic process; mitochondrial membrane organization and biogenesis; negative regulation of Ras protein signal transduction; blastocyst formation; mitochondrion localization; cell cycle arrest; blood coagulation; protein targeting to mitochondrion
Reference #:  O95140 (UniProtKB)
Alt. Names/Synonyms: CMT2A; CMT2A2; CPRP1; HSG; hyperplasia suppressor; KIAA0214; MARF; MFN2; mitochondrial assembly regulatory factor; mitofusin 2; Mitofusin-2; Transmembrane GTPase MFN2
Gene Symbols: MFN2
Molecular weight: 86,402 Da
Basal Isoelectric point: 6.52  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

MFN2

Protein Structure Not Found.


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Sites Implicated In
apoptosis, induced: S27‑p
protein degradation: S27‑p
ubiquitination: S27‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 2 S27-p HMAEVNAsPLKHFVT
0 1 K30 EVNAsPLKHFVTAkK
0 1 K36-ac LKHFVTAkKKINGIF
0 3 K79-ub EEQVLDVkGYLSkVR
0 2 K84-ub DVkGYLSkVRGISEV
0 1 T111 RTSNGKSTVINAMLW
0 2 K154-ub LTEGSEEkRSAkTVN
0 1 K158-ub SEEkRSAkTVNQLAH
0 1 K171-ub AHALHQDkQLHAGSL
1 0 K192-ub NSKCPLLkDDLVLMD
0 1 K243-ac TEKHFFHkVSERLSR
0 1 S249 HkVSERLSRPNIFIL
0 2 K307-ub RIFFVSAkEVLNARI
0 1 K316-ub VLNARIQkAQGMPEG
0 1 K355-ac CISQSAVkTKFEQHT
0 1 K366-ub EQHTVRAkQIAEAVR
0 11 K406-ub DRLKFIDkQLELLAQ
0 3 K416-ub ELLAQDYkLRIkQIt
0 10 K420-ub QDYkLRIkQItEEVE
0 1 T423-p kLRIkQItEEVERQV
1 1 S442 AEEIRRLSVLVDDYQ
0 2 Y448 LSVLVDDYQMDFHPS
0 4 K460-ub HPSPVVLkVYkNELH
0 1 K463-ub PVVLkVYkNELHRHI
0 1 K560-ub VNRFLGPkNSRRALM
0 1 K719 QEIAAMNKkIEVLDS
0 1 K719-ub QEIAAMNkkIEVLDS
0 2 K720-ub EIAAMNkkIEVLDSL
0 1 K730-ub VLDSLQSkAKLLRNk
0 1 K737-ub kAKLLRNkAGWLDSE
  mouse

 
S27 HMAEVNASPLkHFVT
K30-ub EVNASPLkHFVTAKK
K36 LkHFVTAKKKINGIF
K79 EEQVLDVKGYLSkVR
K84-ub DVKGYLSkVRGISEV
T111 RTSNGKSTVINAMLW
K154 LTEGSEEKKSVKTVN
K158 SEEKKSVKTVNQLAH
E171 AHALHQDEQLHAGSM
K192 NSKCPLLKDDLVLMD
K243 TEKQFFHKVSERLsR
S249-p HKVSERLsRPNIFIL
K307 RIFFVSAKEVLSARV
K316 VLSARVQKAQGMPEG
K355 CISQSAVKTKFEQHT
K366 EQHTVRAKQIAEAVR
K406 DRLRFIDKQLELLAQ
K416 ELLAQDYKLRIKQIT
K420 QDYKLRIKQITEEVE
T423 KLRIKQITEEVERQV
S442-p AEEIRRLsVLVDEyQ
Y448-p LsVLVDEyQMDFHPS
K460 HPSPVVLKVYKNELH
K463 PVVLKVYKNELHRHI
K560 VNRFLGPKNSRRALL
K719-m1 QEIAAMNkkVEALDS
K719 QEIAAMNKkVEALDS
K720-ub EIAAMNkkVEALDSL
R730 ALDSLQSRAKLLRNK
K737 RAKLLRNKAGWLDSE
  rat

 
S27 HMAEVNASPLKHFVT
K30 EVNASPLKHFVTAKK
K36 LKHFVTAKKKINGIF
K79-ub EEQVLDVkGYLSKVR
K84 DVkGYLSKVRGISEV
T111-p RTSNGKStVINAMLW
K154 LTEGSEEKKSVKTVN
K158 SEEKKSVKTVNQLAH
E171 AHALHQDEQLHAGSL
K192 NSKCPLLKDGLVLMD
K243 TEKQFFHKVSERLSR
S249 HKVSERLSRPNIFIL
K307 RIFFVSAKEVLSARV
K316 VLSARVQKAQGMPEG
K355 CISQSAVKTKFEQHT
K366 EQHTVRAKQIAEAVR
K406 DRLRFIDKQLELLAQ
K416 ELLAQDYKLRIKQMT
K420 QDYKLRIKQMTEEVE
T423 KLRIKQMTEEVERQV
S442-p AEEIRRLsVLVDEYQ
Y448 LsVLVDEYQMDFHPS
K460 HPSPVVLKVYKNELH
K463 PVVLKVYKNELHRHI
K560 VNRFLGPKNSRRALL
K719 QEIAAMNKKVEALDS
K719 QEIAAMNKKVEALDS
K720 EIAAMNKKVEALDSL
K730 ALDSLQSKAKLLRNK
K737 KAKLLRNKAGWLDSE
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